Kinetics and mechanism of the chemiluminescence associated with the free radical-mediated oxidation of amino acids

Luminescence

Volumn 15, Issue 5, 2000, Pages 273-282

  Aspee A ^a   Lissi, E A ^a  

^a UNIVERSIDAD DE SANTIAGO DE CHILE   (Chile)

Author keywords

2,2 azobis(2 amidino propane) dihydrochloride; Amino acid oxidation; Chemiluminescence; Tryptophan; Tyrosine

Indexed keywords

AMINO ACIDS; FREE RADICALS; OXIDATION; REACTION INTERMEDIATES;

2,2′-AZOBI(2-AMIDINO PROPANE) DIHYDROCHLORIDE; AMINO ACID OXIDATIONS; AMINO-ACIDS; FREE RADICAL SOURCE; KINETICS AND MECHANISM; LIGHT INTENSITY; OXIDATION OF AMINO ACIDS; OXIDATION PROCESS; TRYPTOPHAN; TYROSINE;

CHEMILUMINESCENCE;

AMINO ACID; FREE RADICAL; PERHYDROXYL RADICAL; PEROXIDE; TRYPTOPHAN; TYROSINE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CHEMOLUMINESCENCE; COMPARATIVE STUDY; CONFORMATION; KINETICS; OXIDATION REDUCTION REACTION;

AMINO ACIDS; CHEMILUMINESCENT MEASUREMENTS; FREE RADICALS; KINETICS; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PEROXIDES; TRYPTOPHAN; TYROSINE;

EID: 0034263228     PISSN: 15227235     EISSN: None     Source Type: Journal    
DOI: 10.1002/1522-7243(200009/10)15:5<273::aid-bio591>3.3.co;2-d     Document Type: Article

References (39)

1. 2. Free Rad. Biol. Med. 1986; 2: 135-140.
2. Cadenas E, Varsavsky AI, Boveris A, Chance B. Oxygen or organic hydroperoxide-induced chemiluminescence of brain and liver homogenates. Biochem. J. 1981; 198: 645-654.
3. Boveris A, Cadenas E, Reiter R, Filipkowski M, Nakase Y, Chance B. Organ chemiluminescence: non-invasive assay for oxidative radical reactions. Prod. Natl. Acad. Sci. USA 1980; 77: 347-351.
4. Boveris A, Fraga CG, Varsavsky AI, Koch OR. Increased chemiluminiscence and superoxide production in the liver of chronically ethanol-treated rats. Arch. Biochem. Biophys. 1983; 227: 534-541.
5. Roldán JA, Pinus CR, Turrens JF, Boveris A. Chemiluminescence of ischaemic and reperfused intestine in vivo. Gut 1989; 30: 184-187.
6. Videla JA, Fraga CG, Koch OR. Chemiluminescence of the in situ rat liver after acute ethanol intoxication - effect of (+)-cyanidanol-3. Biochem. Pharmacol. 1983; 32: 2822-2825.
7. Cadenas E, Sies H. Low level chemiluminescence of liver microsomal fractions initiated by tert-butyl hydroperoxide. Eur. J. Biochem. 1982; 124: 349-356.
8. Russell GA. Deuterio-isotope effect in the autoxidation of aralkyl hydrocarbons. Mechanism of the interaction of peroxy radicals. J. Am. Chem. Soc. 1957; 79: 3871-3877.
9. Lissi EA, Cáceres T, Llesuy S, Solari L, Boveris A, Videla LA. On the characteristics of the visible chemiluminescence following free radical lipid peroxidation. Free Rad. Res. Commun. 1989; 6: 293-301.
10. Videla LA, Villena MI, Donoso G, de la Fuente J, Lissi E. Visible chemiluminescence induced by t-butyl hydroperoxide in red blood cell suspensions. Biochem. Int. 1984; 8: 821-830.
11. Lissi EA, Cáceres T, Videla LA. Visible chemiluminescence from rat brain homogenates undergoing autoxidation. II. Kinetics of the luminescence decay. Free Rad. Biol. Med. 1988; 4: 93-97.
12. Lissi EA, Cáceres T, Videla LA. Visible chemiluminescence from rat brain homogenates undergoing autoxidation. I. Effect of additives and products accumulation. Free Rad. Biol. Med. 1986; 2: 63-69.
13. Lissi EA, Franz R, Cabezas J, Fernandez V, Videla LA. Effect of antioxidants and hemoglobin status on the t-butyl hydroperoxide-induced oxygen uptake by red blood cells. Cell Biochem. Funct. 1986; 4: 61-68.
14. Albertini R, Abuja PM. Monitoring of low density lipoprotein oxidation by low-level chemiluminescence. Free Rad. Res. 1998; 29: 75-83.
15. Pollet E, Martinez JA, Metha B, Watts BP, Turrens JF. Role of tryptophan oxidation in peroxynitrite-dependent protein chemiluminescence. Arch. Biochem. Biophys. 1998; 349: 74-80.
16. Watts BP, Barnard M, Turrens J. Peroxynitrite-dependence chemiluminescence of amino acids, proteins, and intact cells. Arch. Biochem. Biophys. 1995; 317: 324-330.
17. Barnard ML, Gurdian S, Diep D, Ladd M, Turrens JF. Protein and amino acid oxidation is associated with increased chemiluminescence. Arch. Biochem. Biophys. 1993; 300: 651-656.
18. Slawinski J, Elbanowski M, Slawinska D. Spectral characteristics and mechanism of chemiluminescence from tryptophan solutions induced by UV-irradiation. Photochem. Photobiol. 1980; 32: 253-260.
19. Escobar JA, Vásquez-Vivar J, Cilento G. Free radicals and excited species in the metabolism of indole-3-acetic acid and its ethyl ester by horseradish peroxidase and by neutrophils. Photochem. Photobiol. 1992; 55: 895-902.
20. Pires de Melo M, Escobar JA, Metodiewa D, Dunford HB, Cilento G. Horseradish peroxidase-catalyzed aerobic oxidation of indole-3-acetic acid. Arch. Biochem. Biophys. 1992; 296: 34-39.
21. Lissi EA, Salim-Hanna M, Fauré M, Videla LA. 2,2′-Azo-bis-amidinopropane as a radical source for lipid peroxidation and enzyme inactivation studies. Xenobiotica 1991; 21: 995-1001.
22. Giulivi C, Davies KJA. Dityrosine: a marker for oxidatively modified proteins and selective proteolysis. Methods Enzymol. 1994; 233: 363-371.
23. Lissi EA, Clavero N. Inactivation of lysozyme by alkylperoxyl radicals. Free Rad. Res. Comm. 1990; 10: 177-184.
24. Lissi EA, Faure M, Clavero N. Effect of additives on the inactivation of lysozyme mediated by free radicals produced in the thermolisis of 2,2′-azo-bis-(2-amidinopropane). Free Rad. Res. Comm. 1991; 14: 373-371.
25. Cilento G. Photochemistry without light. Experientia 1988; 44: 572.
26. Müller A, Cadenas E, Graf P, Sies H. A novel biologically active seleno-organic compound - I. Biochem. Pharmacol. 1984; 33: 3235-3239.
27. Noguchi N, Yasukazu Y, Kaneda H, Yamamoto Y, Niki E. Action of Ebselen as an antioxidant against lipid peroxidation. Biochem. Pharmacol. 1992; 44: 39-44.
28. 2-horseradish peroxidase system: possible formation of tyrosine cation radical. Biochem. Biophys. Res. Commun. 1985; 128: 936-941.
29. Cilento G, Adam W. From free radicals to electronically excited species. Free Rad. Biol. Med. 1995; 19: 103-114.
30. Jin F, Leitich J, von Sonntag C. The superoxide radical reacts with tyrosine-derived phenoxyl radicals by addition rather than by electron transfer. J. Chem. Soc. Perkin Trans. 1993; 2: 1583-1588.
31. Singh SK, Suurkuusk M, Eldsäter C. Kinetics of decomposition of hydroperoxides formed during the oxidation of soya phosphatidylcholine by analysis of chemiluminescence generated. Int. J. Pharmacol. 1996; 142: 215-221.
32. Winterbourn C, Pichorner H, Kettle AJ. Myeloperoxidase-dependent generation of a tyrosine peroxide by neutrophils. Arch. Biochem. Biophys. 1997; 338: 15-21.
33. Friedman M, Cuq JL. Chemistry, analysis, nutritional value, and toxicology of tryptophan in food. A review. J. Agric. Food Chem. 1988; 36: 1079-1093.
34. Shen X, Lind J, Eriksen TE, Menéngi G. The reactions of indoles in aqueous solution initiated by one-electron oxidation. J. Chem. Soc. Perkin Trans. 1990; 2: 597-603.
35. Simat TJ, Steinhart H. Oxidation of free tryptophan and tryptophan residues in peptides and proteins. J. Agric. Food Chem. 1998; 46: 490-498.
36. Nakagawa M, Kato S, Kataoka S, Hino T. 3a-hydroperoxypyrroloindole from tryptophan. Isolation and transformation to formylkynurenine. J. Am. Chem. Soc. 1979; 101: 3136-3137.
37. 3 ring cleavage of tryptophol. Photochem. Photobiol. 1978; 28: 531-534.
38. Gebicki S, Gebicki JM. Formation of peroxides in amino acids and proteins exposed to oxygen free radicals. Biochem. J. 1993; 289: 743-749.
39. 3COO) with tryptophan, tryptophanyl-tyrosine and lysozyme. Int. J. Radiat. Biol. 1981; 39: 135-141.